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Related Concept Videos

Antibody Structure01:10

Antibody Structure

67.3K
Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
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Antibody Structure01:10

Antibody Structure

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Antibody Structure and Classes01:25

Antibody Structure and Classes

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Antibodies, also known as immunoglobulins, are produced by B cells in response to foreign substances, such as bacteria and viruses. These proteins are critical for recognizing and neutralizing these substances, protecting the body from potential harm.
The basic structure of an antibody consists of four protein chains: two identical heavy chains and two identical light chains. These chains are held together by disulfide bonds and other non-covalent interactions, forming a Y-shaped structure.
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Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

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Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
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Conserved Binding Sites01:49

Conserved Binding Sites

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Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
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Diversity of Antigen Receptors01:28

Diversity of Antigen Receptors

2.0K
Antigen receptors are essential components of the immune system crucial in defending the body against foreign invaders. These receptors are present on the surface of B and T cells, enabling them to recognize antigens and mount an appropriate immune response.
Before encountering any antigen, lymphocytes express these receptors. On B cells, the antigen receptor is a membrane-bound antibody molecule called BCR; on T cells, it is a T cell receptor or TCR. B and T cell receptors are composed of two...
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Related Experiment Video

Updated: Mar 25, 2026

Combined Immunofluorescence and DNA FISH on 3D-preserved Interphase Nuclei to Study Changes in 3D Nuclear Organization
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Combined Immunofluorescence and DNA FISH on 3D-preserved Interphase Nuclei to Study Changes in 3D Nuclear Organization

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Ig Constant Region Effects on Variable Region Structure and Function.

Alena Janda1, Anthony Bowen1, Neil S Greenspan2

  • 1Department of Microbiology and Immunology, Albert Einstein College of Medicine New York, NY, USA.

Frontiers in Microbiology
|February 13, 2016
PubMed
Summary
This summary is machine-generated.

Antibodies, or immunoglobulin molecules, traditionally viewed as having independent variable and constant regions, show interconnectedness. Recent research reveals these regions can influence each other, impacting antigen binding and immune function.

Keywords:
constant regionfunctionimmunoglobulinisotypestructurevariable region

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Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding
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Area of Science:

  • Immunology
  • Molecular Biology
  • Biochemistry

Background:

  • The adaptive humoral immune response generates antibodies (immunoglobulin molecules) for defense against pathogens.
  • Antibodies possess variable regions for antigen binding and constant regions for effector functions like opsonization.
  • These regions were historically considered structurally and functionally independent.

Purpose of the Study:

  • To review the evidence demonstrating interdependence between antibody variable and constant regions.
  • To explore proposed mechanisms for the interaction between these antibody domains.

Main Methods:

  • Review of existing scientific literature.
  • Analysis of experimental data on antibody structure-function relationships.

Main Results:

  • Emerging evidence indicates that in certain antibody families, variable and constant regions are not independent.
  • These regions can influence each other's function, particularly in antigen binding.

Conclusions:

  • The traditional view of independent antibody domains requires revision.
  • Interactions between variable and constant regions represent a key area for understanding antibody function and regulation.